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J Bacteriol. 1968 March; 95(3): 983-985
Copyright © 1968 American Society for Microbiology. All Rights Reserved.
1 Department of Developmental Biology, Institute of Biological and Medical Sciences, Retina Foundation, Boston, Massachusetts 02114
ABSTRACT
The stability of uridine diphosphoglucose pyrophosphorylase was examined in extracts prepared at different stages of development in Dictyostelium discoideum. In the early stages, the kinetics of inactivation were nonlinear, and, therefore, it was not possible to determine the specific enzyme activity. In the later stages of development, the enzyme was stable, but it could be rapidly inactivated by a heat-labile inhibitor present in extracts prepared at an early stage.
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